ID A0A0B7N103_9FUNG Unreviewed; 1094 AA.
AC A0A0B7N103;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=PARPA_05833.1 scaffold 20154 {ECO:0000313|EMBL:CEP11926.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP11926.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP11926.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP11926.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000256|ARBA:ARBA00007296}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; LN727218; CEP11926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7N103; -.
DR STRING; 35722.A0A0B7N103; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProt.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd18175; ATP-synt_Vo_c_ATP6C_rpt1; 1.
DR CDD; cd18176; ATP-synt_Vo_c_ATP6C_rpt2; 1.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR015063; USP8_dimer.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR NCBIfam; TIGR01100; V_ATP_synt_C; 1.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF95; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4-RELATED; 1.
DR Pfam; PF00137; ATP-synt_C; 2.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 939..961
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 981..1008
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1020..1046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1058..1082
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 256..376
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 597..931
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 134..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 121013 MW; CAF3C859E939F99A CRC64;
MTVPTSGGVP SPPSHSLAEL SRRATVDKTD MSKYSFRSWI TTVCKLYEQG DFEYLQNSLD
EAYVYYMKGC SIMVEVIAKH QDYKEAKKDT TYRQLKARTN DDILMRLEEI SMKLQHDDHD
QPENDFVQEA MTRYPPIDDM PTPSPISIGS NSFLDSLPSV PTHIPKNDDT QARLANRKDS
GGGSSSSSFN SSSSSSPVNF MKMPEPEHQP QPQQPMPVTT IRLQLPTPSS EFAITPTPIV
DPRQLASWIV KKNDVKQPSV LILDVRPRQT FEQGSIKHRW IAQIEPLVLK QDVCSQKIEE
SMIMNPDAEQ QIFAGRNQFD LIVYYDQNSQ TLQNETLAHL HAAIYELEFK KILQRAPVML
AGGFDAWRQV IGEKGIFRYN VGNDLASSSA STSSQGVPSQ HKSHWLKDVV GKGSDQSSLT
AVKVHHTFYD YFSSSGSSGT KESMTRHIGR NVATPPLRGV FSNTLYQPSN APTTTHTMPI
PQPAPSTALE AEKSSIRYPE IQPNMSKLQR KKTFIDNPFH GFTSTTNQQF EVPPLPPKPQ
RPLPPVPAAA TTAVVPSAPP LPPKEPYASS PTDNAYRTAP VSDNSFSQMS TVLIGTTGLK
NLGNTCFMNS IIQCLSGTIP FARYFISGVF RQHINKDNFL GTGGVLAENF SSLLRTMWSE
NYNFISPVLF REALIKFAPQ FRGSEQHDSQ EFLNFLLDGI HEDCNLVRKR PTPPPESAEE
EARFELLPDW KASAIAWERY LERNSSVVVS LFQGQYRSRL TCLTCHATST TYNSFMSLSL
PIPAKRSGPP SVSIYQCLDY FVKEEILDND DAWQCPKCKT LRRASKALTL SKLPDVLLIH
LKRFSFDGPF KDKLETIVES PMRQPPEKSA FKYDLYAVSN HFGSLTGGHY TACVRNGYKN
EWHNFDDSRF SVCDDSKVLS RAAYNLFYVR STMSEYCPVY APFFGTMGCA AAIVFSCLGA
AYGTAKSGVG LSAMGVLRPD LVLKCIVPVV MAGILGIYGV VVSVLLSGGL AMKQTLFSGF
IQMAAGLSVG LSCLAAGIAI GITGDAGVRA TAQQPRMFVG MILILIFAEV LGLYGLIVAL
ILNTKASGQE NVCS
//
